5KHN

Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN

5KHN の概要

• エントリーDOI: 10.2210/pdb5khn/pdb
• 関連するPDBエントリー: 5KHS
• 分子名称: RND transporter (1 entity in total)
• 機能のキーワード: transmembrane helices, membrane protein
• 由来する生物種: Burkholderia multivorans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 187002.95

構造登録者

Su, C.-C.,Yu, E.W. (登録日: 2016-06-15, 公開日: 2017-06-14, 最終更新日: 2024-03-06)

主引用文献

Kumar, N.,Su, C.C.,Chou, T.H.,Radhakrishnan, A.,Delmar, J.A.,Rajashankar, K.R.,Yu, E.W.
Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN.
Proc. Natl. Acad. Sci. U.S.A., 114:6557-6562, 2017

PubMed Abstract: Strains of the complex (Bcc) are Gram-negative opportunisitic bacteria that are capable of causing serious diseases, mainly in immunocompromised individuals. Bcc pathogens are intrinsically resistant to multiple antibiotics, including β-lactams, aminoglycosides, fluoroquinolones, and polymyxins. They are major pathogens in patients with cystic fibrosis (CF) and can cause severe necrotizing pneumonia, which is often fatal. Hopanoid biosynthesis is one of the major mechanisms involved in multiple antimicrobial resistance of Bcc pathogens. The gene of encodes an integral membrane protein of the HpnN family of transporters, which is responsible for shuttling hopanoids to the outer membrane. Here, we report crystal structures of HpnN, revealing a dimeric molecule with an overall butterfly shape. Each subunit of the transporter contains 12 transmembrane helices and two periplasmic loops that suggest a plausible pathway for substrate transport. Further analyses indicate that HpnN is capable of shuttling hopanoid virulence factors from the outer leaflet of the inner membrane to the periplasm. Taken together, our data suggest that the HpnN transporter is critical for multidrug resistance and cell wall remodeling in .

PubMed: 28584102
DOI: 10.1073/pnas.1619660114

実験手法

X-RAY DIFFRACTION (3.445 Å)